Abstract
Transient receptor potential vanilloid channel 3 (TRPV3), a member of the thermosensitive TRP (thermoTRPV) channels, is activated by warm temperatures and serves as a key regulator of normal skin physiology through the release of pro-inflammatory messengers. TRPV3 sensitizes upon repeated stimulation, yet a lack of structural information about the channel precludes a molecular-level understanding of TRPV3 sensitization and gating. Here, we present the cryo-electron microscopy structures of apo and sensitized human TRPV3, as well as several structures of TRPV3 in the presence of the common thermoTRPV agonist 2-aminoethoxydiphenyl borate (2-APB). Our results show α-to-π-helix transitions in the S6 during sensitization, and suggest a critical role for the S4-S5 linker π-helix during ligand gating.
Highlights
2658-Pos Activation of transient receptor potential vanilloid receptor 1 (TRPV1) by Lipids: Can Lipid Tails Bridge the Gap between the Vanilloid Binding Site and the Peripheral Cavities? Eleonora Gianti1, Michael L
Transient receptor potential canonical 3 (TRPC3) forms non-selective cation channels that are opened in response to phospholipase C stimulation
The permeability ratio PCa2þ/PCsþ was close to 3 for TRPC3 pores opened via phospholipase C stimulation or photoisomerization of OptoDArG, but 0.8 for channels activated by photoisomerization of OptoBI-1
Summary
2658-Pos Activation of TRPV1 by Lipids: Can Lipid Tails Bridge the Gap between the Vanilloid Binding Site and the Peripheral Cavities? Eleonora Gianti1, Michael L. Transient receptor potential canonical 3 (TRPC3) forms non-selective cation channels that are opened in response to phospholipase C stimulation. This physiologic mode of activation involves a direct interaction of diacylglycerols with residues within a lateral fenestration of the pore domain behind the selectivity filter.
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